LAP1_UNCRE
ID LAP1_UNCRE Reviewed; 395 AA.
AC C4JLL1;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Leucine aminopeptidase 1;
DE EC=3.4.11.-;
DE AltName: Full=Leucyl aminopeptidase 1;
DE Short=LAP1;
DE Flags: Precursor;
GN Name=LAP1; ORFNames=UREG_03719;
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- FUNCTION: Extracellular aminopeptidase that allows assimilation of
CC proteinaceous substrates. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily.
CC {ECO:0000305}.
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DR EMBL; CH476616; EEP78873.1; -; Genomic_DNA.
DR RefSeq; XP_002544202.1; XM_002544156.1.
DR AlphaFoldDB; C4JLL1; -.
DR SMR; C4JLL1; -.
DR STRING; 33188.XP_002544202.1; -.
DR MEROPS; M28.022; -.
DR EnsemblFungi; EEP78873; EEP78873; UREG_03719.
DR GeneID; 8439582; -.
DR KEGG; ure:UREG_03719; -.
DR VEuPathDB; FungiDB:UREG_03719; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_025866_0_0_1; -.
DR InParanoid; C4JLL1; -.
DR OrthoDB; 1257666at2759; -.
DR Proteomes; UP000002058; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW Protease; Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..95
FT /evidence="ECO:0000250"
FT /id="PRO_0000412452"
FT CHAIN 96..395
FT /note="Leucine aminopeptidase 1"
FT /id="PRO_0000412453"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 329..333
FT /evidence="ECO:0000250"
SQ SEQUENCE 395 AA; 43702 MW; 1639D034BCC9ED69 CRC64;
MKHLSLLALA AVAPTTALAG VIDHQQVTFE KPPTHNQIEK FLIQLGPGES RWVTEEEKWA
LKLVGFYVLE GMNFFDITAE SDQGFSVKSF EQTKVTYPSE IKYQKELAPL SKDLSKGNMR
ENLVKFTSFH TRYYKSETGV QSATWLLERV QQAIDDSGAS KHGVKVEKFN HPWGQFSIIA
TIPGRSNKTV VVGAHQDSIN LFLPSILAAP GADDDGSGTV TILEAFRVLL QSDAIREGKA
ANTVEFHWYS AEEAGLLGSQ AIFSEYSKTG RDVKAMLQQD MTGYVEGTLR AGEVESVGVI
TDFVDPGLTE FIKLVIKGYC DIPFVLTKCG YACSDHASAS RYGYPSAFVI ESEFKRSNQK
IHTTSDTIEL LSFDHMLQHA KMTLGLAYEL AFAEL
